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- W2150352010 abstract "A psychrotrophic bacterium Shewanella sp. strain SIB1 was grown at 4 and 20 °C, and total soluble proteins extracted from the cells were analyzed by two‐dimensional polyacrylamide gel electrophoresis. Comparison of these patterns showed that the cellular content of a protein with a molecular mass of 28 kDa and an isoelectric point of four greatly increased at 4 °C compared to that at 20 °C. Determination of the N‐terminal amino acid sequence, followed by the cloning and sequencing of the gene encoding this protein, revealed that this protein is a member of the FKBP family of proteins with an amino acid sequence identity of 56% to Escherichia coli FKBP22. This protein was overproduced in E. coli in a His‐tagged form, purified, and analyzed for peptidyl‐prolyl cis‐trans isomerase activity. When this activity was determined by the protease coupling assay using N ‐succinyl‐Ala‐Leu‐Pro‐Phe‐ p ‐nitroanilide as a substrate at various temperatures, the protein exhibited the highest activity at 10 °C with a k cat / K m value of 0.87 µ m −1 ·s −1 . When the peptidyl‐prolyl cis‐trans isomerase activity was determined by the RNase T 1 refolding assay at 10 and 20 °C, the protein exhibited higher activity at 10 °C with a k cat / K m value of 0.50 µ m −1 ·s −1 . These k cat / K m values are lower but comparable to those of E. coli FKBP22. We propose that a FKBP family protein is involved in cold‐adaptation of psychrotrophic bacteria." @default.
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- W2150352010 date "2004-03-23" @default.
- W2150352010 modified "2023-10-17" @default.
- W2150352010 title "Possible involvement of an FKBP family member protein from a psychrotrophic bacterium Shewanella sp. SIB1 in cold-adaptation" @default.
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- W2150352010 doi "https://doi.org/10.1111/j.1432-1033.2004.04049.x" @default.
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